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. Author manuscript; available in PMC: 2013 Sep 16.
Published in final edited form as: Biochemistry. 2010 Jan 12;49(1):195–206. doi: 10.1021/bi901614m

Figure 4.

Figure 4

(a) Superposition of the E. coli and Sp9 DHFR monomers colored according to their temperature factors with red representing mobile regions and blue, the rigid regions. The substrate binding loops and helix in the E. coli structure seem to be more flexible compared to the Sp9 mutant. (b) Cartoon representation of the Sp9 DHFR dimer. (c) Stereo view of the dimer interface. Residues are shown in stick representation.